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Protein

Fructose-bisphosphate aldolase 1

Gene

cfxA

Organism
Rhodobacter sphaeroides (Rhodopseudomonas sphaeroides)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

Functioni

Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis.By similarity

Miscellaneous

This protein is encoded within the form I ribulose-bisphosphate carboxylase operon, which predominates when carbon dioxide is limiting.

Catalytic activityi

D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate.

Cofactori

Zn2+By similarityNote: Binds 2 Zn2+ ions per subunit. One is catalytic and the other provides a structural contribution.By similarity

Pathwayi: Calvin cycle

This protein is involved in the pathway Calvin cycle, which is part of Carbohydrate biosynthesis.
View all proteins of this organism that are known to be involved in the pathway Calvin cycle and in Carbohydrate biosynthesis.

Pathwayi: glycolysis

This protein is involved in step 4 of the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Glucose-6-phosphate isomerase (pgi)
  3. no protein annotated in this organism
  4. Fructose-1,6-bisphosphate aldolase (B6K69_09500), Fructose-bisphosphate aldolase 1 (cfxA), Fructose-bisphosphate aldolase 2 (cfxB)
This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose, the pathway glycolysis and in Carbohydrate degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei50Glyceraldehyde 3-phosphateBy similarity1
Active sitei83Proton donorBy similarity1
Metal bindingi84Zinc 1; catalyticBy similarity1
Metal bindingi105Zinc 2By similarity1
Metal bindingi142Zinc 2By similarity1
Metal bindingi198Zinc 1; catalyticBy similarity1
Binding sitei199Dihydroxyacetone phosphate; via amide nitrogenBy similarity1
Metal bindingi232Zinc 1; catalyticBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionLyase
Biological processCalvin cycle, Glycolysis
LigandMetal-binding, Zinc

Enzyme and pathway databases

UniPathwayi
UPA00109;UER00183

UPA00116

Names & Taxonomyi

Protein namesi
Recommended name:
Fructose-bisphosphate aldolase 1 (EC:4.1.2.13)
Short name:
FBP aldolase
Short name:
FBPA
Alternative name(s):
Fructose-1,6-bisphosphate aldolase
Fructose-bisphosphate aldolase I
Gene namesi
Name:cfxA
OrganismiRhodobacter sphaeroides (Rhodopseudomonas sphaeroides)
Taxonomic identifieri1063 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001787311 – 359Fructose-bisphosphate aldolase 1Add BLAST359

Interactioni

Subunit structurei

Homodimer.

Structurei

3D structure databases

ProteinModelPortaliP27995
SMRiP27995
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni233 – 235Dihydroxyacetone phosphate bindingBy similarity3
Regioni275 – 278Dihydroxyacetone phosphate bindingBy similarity4

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105D2N Bacteria
COG0191 LUCA

Family and domain databases

CDDicd00947 TBP_aldolase_IIB, 1 hit
Gene3Di3.20.20.70, 1 hit
InterProiView protein in InterPro
IPR013785 Aldolase_TIM
IPR000771 FBA_II
IPR006412 Fruct_bisP_Calv
PfamiView protein in Pfam
PF01116 F_bP_aldolase, 1 hit
PIRSFiPIRSF001359 F_bP_aldolase_II, 1 hit
TIGRFAMsiTIGR00167 cbbA, 1 hit
TIGR01521 FruBisAldo_II_B, 1 hit
PROSITEiView protein in PROSITE
PS00602 ALDOLASE_CLASS_II_1, 1 hit
PS00806 ALDOLASE_CLASS_II_2, 1 hit

Sequencei

Sequence statusi: Complete.

P27995-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MALITLRQLL DHAAERLQGY GVPAFNINNM EQGLAILAAA RACDAPVIAS
60 70 80 90 100
RGARSYAGDI MLRHIVEALA EMYPQIPICL HQDHGNNEAT CLSAIRHGFT
110 120 130 140 150
SVMMDGSLQA DMKTVASYDY NVDITRRVTD AAHWVGASVE GELGVLGSLE
160 170 180 190 200
KGEAEAEDGS GAEGKLDHSQ MLTDPDQAVE FVQATRVDAL AIAMGTSHGA
210 220 230 240 250
YKFSRKPDGE ILAMRVIEEI HARLPATHLV MHGSSSVAAR LQDLINAHGA
260 270 280 290 300
DMPQTYGVPV EEIERGIRHG VRKVNIDTDC RMALTGQFRK VAMESPKEFD
310 320 330 340 350
ARKFMIPAMK EMEALVRDRF ERFGTAGNAS KITVIPMDDM AKRYASGALD

PAVATAKAA
Length:359
Mass (Da):38,872
Last modified:August 1, 1992 - v1
Checksum:i6A898301D5A2F1ED
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64624 Genomic DNA Translation: AAA26114.1
PIRiB40767 ADRFAS

Similar proteinsi

Entry informationi

Entry nameiALF1_RHOSH
AccessioniPrimary (citable) accession number: P27995
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: July 5, 2017
This is version 76 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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